PTRH2 Human
Peptidyl-tRNA Hydrolase 2 Human Recombinant
Cat. No.
BT28964
Source
Escherichia Coli.
Synonyms
Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
PTRH2 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 137 amino acids (64-179 a.a.) and having a molecular mass of 14.9kDa. The PTRH2 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Peptidyl-tRNA hydrolase 2, also known as PTRH2, is a mitochondrial protein that plays a role in apoptosis (programmed cell death). During apoptosis, PTRH2 is released from the mitochondria into the cytoplasm. Once in the cytoplasm, PTRH2 regulates two transcriptional regulators, TLE5 and TLE1, which promotes caspase-independent cell death. PTRH2 is thought to act on peptidyl-tRNAs that detach from the ribosome during protein synthesis.
Description
This product consists of the recombinant human PTRH2 protein, expressed in E. coli bacteria. A 21 amino acid His tag is fused to the N-terminus of the protein to facilitate purification. The resulting protein is a single, non-glycosylated polypeptide chain containing 137 amino acids (residues 64-179 of the full-length protein) with a molecular weight of 14.9 kDa. The PTRH2 protein is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The PTRH2 protein is supplied in a solution containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, and 1mM DTT at a concentration of 1 mg/ml.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the product frozen at -20°C. Adding a carrier protein such as 0.1% HSA or BSA is recommended for long-term storage. Avoid repeated freezing and thawing of the product.
Purity
The purity of the PTRH2 protein is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEYKMILVVR NDLKMGKGKV AAQCSHAAVS AYKQIQRRNP EMLKQWEYCG QPKVVVKAPD EETLIALLAH AKMLGLTVSL IQDAGRTQIA PGSQTVLGIG PGPADLIDKV TGHLKLY.
Product Science Overview
Structure and Localization
PTRH2 is characterized by two main domains:
- N-terminal mitochondrial localization sequence: This sequence directs the protein to the mitochondria.
- UPF0099 domain: This domain is essential for its enzymatic activity.
Function
Role in Cell Survival and Death
PTRH2 is involved in regulating cell survival and apoptosis:
- Cell Survival: It promotes cell survival as part of an integrin-signaling pathway for cells attached to the extracellular matrix (ECM).
- Apoptosis: In cells that have lost their attachment to the ECM, a process known as anoikis, PTRH2 promotes apoptosis. Upon loss of cell attachment, PTRH2 is phosphorylated, released from the mitochondria into the cytosol, and promotes caspase-independent apoptosis through interactions with transcriptional regulators .
Clinical Significance
Mutations in the PTRH2 gene have been associated with a rare autosomal recessive disorder known as Infantile Multisystem Neurologic, Endocrine, and Pancreatic Disease (IMNEPD). This disorder is characterized by:
Research and Applications
Due to its significant role in cellular processes and disease, PTRH2 is a subject of ongoing research. Understanding its mechanisms can provide insights into potential therapeutic targets for related disorders and conditions.
Quick Inquiry
Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
